Ultrastructural localization of antigenic sites on osmium-fixed tissues applying the protein A-gold technique.

Bendayan, Moı̈se; Zollinger, Max

doi:10.1177/31.1.6187796

Cited by 622 publications

(261 citation statements)

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“…Before labeling, ultrathin sections were pretreated for 1 hour in a saturated aqueous solution of sodium metaperiodate (18). One side of the grids was then incubated at 37°C for 12 hours with specific antisera directed toward either GH or PRL.…”

Section: Ultrastructural Studiesmentioning

confidence: 99%

Reversible Transdifferentiation: Interconversion of Somatotrophs and Lactotrophs in Pituitary Hyperplasia

et al. 2001

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Previous studies conclusively demonstrated transformation of somatotrophs into bihormonal mammosomatotrophs in gestational lactotroph hyperplasia during pregnancy. Similar transdifferentiation of somatotrophs into thyrotrophs through bihormonal intermediate thryrosomatotrophs was documented during thyrotroph hyperplasia in both rodent and human pituitaries in hypothyroidism. The cessation of the stimulation resulted in reversal of the process in both conditions. The conversion of lactotrophs into somatotrophs was suggested but not documented previously in the human gland. The present study was undertaken to investigate cases of somatotroph hyperplasia by transmission electron microscopy, immunoelectron microscopy using double immunogold labeling for growth hormone and prolactin, as well as combined immunocytochemistry and in situ hybridization. Adenohypophysial tissue was removed from a 38-year-old man and a 29-year-old woman with longstanding acromegaly due to ectopic overproduction of growth hormone-releasing hormone (GRH) by bronchial carcinoid tumors. For comparison, two pituitary biopsies were studied: one from a 38-year old woman with idiopathic lactotroph hyperplasia and one from a 14-year-old boy with secondary lactotroph hyperplasia due to a suprasellar craniopharyngioma. In the patients with somatotroph hyperplasia, the prevailing cell type was the hyperplastic somatotroph joined by mammosomatotroph deriving from lactotrophs, whereas monohormonal lactotrophs were rare. The predominance of mammosomatotrophs and active lactotrophs was documented in the patient with idiopathic lactotroph hyperplasia, whereas the case of the patient with secondary lactotroph hyperplasia was characterized by monohormonal lactotrophs and somatotrophs, but mammosomatotrophs were rare. That finding in the pituitary of the boy suggests that participation of mammosomatotrophs in lactotroph hyperplasia is not unconditional. Our findings conclusively demonstrate conversion of lactotrophs into mammosomatotrophs during somatotroph hyperplasia, providing further evidence for the potential of reversible transdifferentiation between somatotrophs and lactotrophs in response to functional demand.

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Section: Ultrastructural Studiesmentioning

confidence: 99%

Reversible Transdifferentiation: Interconversion of Somatotrophs and Lactotrophs in Pituitary Hyperplasia

et al. 2001

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“…Thus, cryosectioning techniques were not applicable in this study. Recent advances in postembedding immunolabeling using sections of plastic embedded tissues (3,(11)(12)(13) prompted the use of more conventional fixation, dehydration, and embedding methods for the study of the subcellular localization of phaseolin in mature seed tissues from transformed tobacco. The results of this investigation illustrate that high resolution localization of antigens at both the light and electron microscopic levels can be successfully performed using sections of conventionally prepared plant tissues.…”

mentioning

confidence: 99%

Correct Targeting of the Bean Storage Protein Phaseolin in the Seeds of Transformed Tobacco

Greenwood¹,

Chrispeels²

1985

Plant Physiol.

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“…The antibodies to CPS bound only to ER in close proximity to mitochondria. The labelling of CPS on ER adjacent to mitochondria can also be seen in the osmium tetroxide fixed sections of Bendayan and Zollinger (1983).…”

Section: Clustering Of Cps In the Cytoplasm And Mitochondrial Matrixmentioning

confidence: 80%

Import of Carbamylphosphate Synthetase and Ornithine Transcarbamylase Into Mitochondria of Rat Liver: Detection of Aggregates of Enzyme in Cytoplasm and Mitochondria Using Immunoelectron Microscopy With the Protein A‐gold Method

Brands

Hoogenraad

1986

Aust J Exp Biol Med

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Summary.We investigated the distribution of the nuclear encoded mitochondrial enzymes, carbamylphosphate synthetase (CPS; EC 6.3.4.16) and ornithine transcarbamylase (OTC; EC 2.1.3.3) in liver by immunocytochemistry on ultrathin sections using the protein A-gold technique. Both enzymes were found to be present as aggregates in the cytoplasm of hepatocytes, in association with ER membranes adjacent to mitochondria. Clusters of the enzymes were also found inside the mitochondria. The aggregation of these enzymes was found only with antibodies to CPS and OTC and not with antibodies against albumin or with IgG from unimmunized serum, nor were aggregates found in cells other than hepatocytes. The results are suggestive of localized uptake of clusters of enzyme or co-translational uptake of enzyme at discrete localizations and that endoplasmic reticulum (ER) associations may be necessary for uptake of the precursor forms of CPS and OTC. The possible involvement is discussed of micropinosomes which are seen associated with inner membrane, intermembrane space and outer membrane in mitochrondria obtained from a perinuclear pellet where ER and mitochondria are frequently found in close association.

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Ultrastructural localization of antigenic sites on osmium-fixed tissues applying the protein A-gold technique.

Cited by 622 publications

References 0 publications

Reversible Transdifferentiation: Interconversion of Somatotrophs and Lactotrophs in Pituitary Hyperplasia

Reversible Transdifferentiation: Interconversion of Somatotrophs and Lactotrophs in Pituitary Hyperplasia

Correct Targeting of the Bean Storage Protein Phaseolin in the Seeds of Transformed Tobacco

Import of Carbamylphosphate Synthetase and Ornithine Transcarbamylase Into Mitochondria of Rat Liver: Detection of Aggregates of Enzyme in Cytoplasm and Mitochondria Using Immunoelectron Microscopy With the Protein A‐gold Method

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